Timothy Ray Brown (aka, The Berlin Patient) is the first person to go from being HIV+ to HIV-. Usually, he's described as the first person to be cured of AIDS. Scientists are a bit more circumspect about the situation. Brown got a bone marrow transplant using marrow donated by a person whose body has natural resistance to HIV. That was in 2005. Now off of anti-retroviral drugs, Brown's HIV has (so far) not returned. Two other men have been through the same treatment with promising results, although they are still taking anti-retroviral drugs, so it's impossible to say yet whether they are also actually HIV-.

Even if this is a cure, it is not the world's most widely applicable cure. Yet. But it is very interesting and, obviously, an amazing story.

I've never heard Timothy Ray Brown speak before, so I wanted to post this interview video from Democracy Now. It probably won't add much to the story that you didn't already know, but it's powerful to see the guy, himself, talking about it.

PREVIOUSLY

We've talked here before about the importance of the protein CCR5 in HIV/AIDS treatment research. CCR5 is a protein on the surface of immune cells. Some people have a genetic mutation, called Delta-32, which alters how that protein works, how often it appears, or changes its structure. People with the mutation have immunity to some strains of HIV, the virus that causes AIDS.

CCR5 is the key to the Berlin Patient—Timothy Ray Brown—who, until recently, was the only person to ever be cured of AIDS. Brown received bone marrow transplants from people who had the Delta-32 mutation. His body has been HIV-free for five years. And, last week, researchers announced that two other people successfully received the same treatment.

But here's the thing, until today, I didn't totally understand how the connection between CCR5, Delta-32, and HIV worked. There's a story (and some great digital illustrations) on NPR's Shots blog that makes the situation much more clear. HIV, apparently, have little spikes all over its surface. These spikes are how the virus injects itself into cells.

When it bumps into a T cell, a finger-like projection on the cell's surface, called CCR5, pushes down on the spike. This interaction pops open the HIV and releases the infectious genes into the cell. A gene therapy could protect T cells by inactivating the CCR5 gene.

Great "A-ha!" moment for me. Read the rest of the story and look at the illustrations. It'll make some thing make a lot more sense.

Read the rest at NPR's Shots blog

PREVIOUSLY:
If AIDS Has Been Cured, Why is the Victory Party So Small?
AIDS Research Done by 17-Year-Olds

Fifteen years ago, Dr. Harry Kestler got a call from a colleague in Florida who had inadvertently stumbled across a very unique family. An African-American woman had brought her sick child into the hospital only to discover that the child was HIV-positive and experiencing symptoms of AIDS. Further tests showed that she, herself, had HIV. As did four of her five children. It was a family tragedy. But in the midst of that, Kestler's colleague had noticed something odd.

The woman knew how she must have been infected—her ex-husband had been an intravenous drug user. But that had been more than 20 years ago. She, and her oldest child, had had HIV for over two decades without developing any symptoms. And her second-oldest child—who shared the same father—wasn't infected with HIV at all.

I've written here before about long-term non-progressors—a rare class of people who can be infected with HIV and live for decades without the virus ever developing into anything serious. Their secret: mutations in their genes that prevent HIV from binding to cells, which means it can't invade the cells or replicate.

Yesterday at the American Association for the Advancement of Science conference, I visited the student poster session, a place where undergraduate college students present research projects they're involved in and compete against one another to earn their poster a spot in an upcoming issue of the journal Science. There, among undergrads from MIT, Harvard, and other prestigious institutions, I met some surprising entrants. Eric McCallister—a student at Ohio's Lorain County Community College—and Megan Sheldon and Conner Anderson—two teenagers who go to high school at the same community college. All three of them are working with Harry Kestler to study the mutations that protect HIV non-progressors against an otherwise deadly virus. Unique researchers studying a unique family.

Read the rest

From Ethan Persoff's ongoing chronicles of vintage weird ephemera: COMICS WITH PROBLEMS #7 - MADONNA ON AIDS. This public health pamphlet was handed out at one of her concerts, one night only, in 1987. Her image appears on the cover, and inside, a handwritten note urging for greater awareness of AIDS and an end to prejudice against those who contract it (or who are HIV-positive).

A couple of years ago, I told you about Foldit, a computer game that harnesses the power of human putzing to help scientists unravel the mysteries of protein structure. There's a new research paper out that uses results from Foldit as a basis for a new proposed structure of a key protein in a virus that is a relative of HIV.

As important as proteins are, we know relatively little about how and why these complex chains of amino acids fold and twist the way they do and how that structure relates to function. Foldit takes advantage of the fact that, given the right rules, people can come up with possible, plausible protein structures far faster than a computer program can factor out all the possible permutations. And that's why Foldit players—citizen scientists of a sort—were so useful in this case. Ed Yong at Not Exactly Rocket Science explains:

They discovered the structure of a protein belonging to the Mason-Pfizer monkey virus (M-PMV), a close relative of HIV that causes AIDS in monkeys. These viruses create many of their proteins in one big block. They need to be cut apart, and the viruses use a scissor enzyme –a protease – to do that. Many scientists are trying to find drugs that disable the proteases. If they don’t work, the virus is hobbled – it’s like a mechanic that cannot remove any of her tools from their box.

To disable M-PMV’s protease, we need to know exactly what it looks like. Like real scissors, the proteases come in two halves that need to lock together in order to work. If we knew where the halves joined together, we could create drugs that prevent them from uniting. But until now, scientists have only been able to discern the structure of the two halves together. They have spent more than ten years trying to solve structure of a single isolated half, without any success.

The Foldit players had no such problems. They came up with several answers, one of which was almost close to perfect. In a few days, Khatib had refined their solution to deduce the protein’s final structure, and he has already spotted features that could make attractive targets for new drugs.

“This is the first instance that we are aware of in which online gamers solved a longstanding scientific problem,” writes Khatib. “These results indi­cate the potential for integrating video games into the real-world scientific process: the ingenuity of game players is a formidable force that, if properly directed, can be used to solve a wide range of scientific problems.”